Oryzacystatin-II, a cystatin from rice (Oryza sativa L. japonica), is a dimeric protein: possible involvement of the interconversion between dimer and monomer in the regulation of the reactivity of oryzacystatin-II.

We examined the biochemical and structural properties of oryzacystatin-II, a phytocystatin in rice (Oryza sativa L. japonica), under heat-stress conditions. The enzyme inhibitory reactivity of oryzacystatin-II was enhanced by heating in a temperature-dependent manner and reached a maximum level by heating at 65 degrees C for 10 min. Size-exclusion chromatography showed that oryzacystatin-II forms a homodimer at ambient temperature and that the enhancement of inhibitory reactivity is due to the conversion of the dimeric to a monomeric form. The monomeric form of oryzacystatin-II reverted to the dimer during storage at 4 degrees C, suggesting that dimerization is an intrinsic property of oryzacystatin-II. The affinity of the monomer for cysteine proteinases was significantly higher than that of the dimer. This is the first paper to describe the noncovalent dimerization for a cystatin under nonstress conditions.